scholarly journals Purification and characterization ofKlebsiella aerogenesUreE protein: A nickel-binding protein that functions in urease metallocenter assembly

1993 ◽  
Vol 2 (6) ◽  
pp. 1042-1052 ◽  
Author(s):  
Mann Hyung Lee ◽  
H. Stuart Pankratz ◽  
Shengke Wang ◽  
Robert A. Scott ◽  
Michael G. Finnegan ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Purification And Characterization ◽  
Metallocenter Assembly ◽  
Nickel Binding

Purification and Characterization of the Periplasmic Nickel-Binding Protein NikA of Escherichia coli K12

1995 ◽  
Vol 227 (3) ◽  
pp. 857-865 ◽  
Author(s):  
Karinne Pina ◽  
Clarisse Navarro ◽  
Laura Mcwalter ◽  
David H. Boxer ◽  
Nicholas C. Price ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Purification And Characterization ◽  
Escherichia Coli K12 ◽  
Nickel Binding

scholarly journals Purification and Characterization of the Periplasmic Nickel-Binding Protein NikA of Escherichia coli K12

2008 ◽  
Vol 227 (3) ◽  
pp. 857-865 ◽  
Author(s):  
Karinne Pina ◽  
Clarisse Navarro ◽  
Laura Mcwalter ◽  
David H. Boxer ◽  
Nicholas C. Price ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Purification And Characterization ◽  
Escherichia Coli K12 ◽  
Nickel Binding

Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum
Keyword(s):  
Actin Filaments ◽  
High Speed ◽  
Binding Protein ◽  
Protein A ◽  
Actin Binding ◽  
Platelet Glycoprotein ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Triton X ◽  
Calpain Inhibitors

SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP interaction resides in the 90 kDa region of ABP. GP lb was sedimented with the Triton-insoluble actin filaments in trace amounts only, and only after high speed centrifugation (100,000 × g, 3 h). Both the 190 kDa and the 90 kDa fragments of ABP were sedimented with the Triton-insoluble actin filaments.

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